JBC PeproTech; Our Business is Cytokines!

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/jbc.M106927200 on September 28, 2001

J. Biol. Chem., Vol. 276, Issue 50, 46792-46797, December 14, 2001
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
276/50/46792    most recent
M106927200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Driggers, P. H.
Right arrow Articles by Rubino, D. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Driggers, P. H.
Right arrow Articles by Rubino, D. M.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

The Proto-oncoprotein Brx Activates Estrogen Receptor beta  by a p38 Mitogen-activated Protein Kinase Pathway*

Paul H. DriggersDagger ||§, James H. Segars, and Domenica M. RubinoDagger

From the Dagger  Department of Obstetrics and Gynecology, Uniformed Services University of the Health Sciences, Bethesda, Maryland 20814, || United States Military Cancer Institute, Bethesda, Maryland 20814, and the  Pediatric and Reproductive Endocrinology Branch, NICHD, National Institutes of Health, Bethesda, Maryland 20892

The estrogen receptors (ERs) are ligand-inducible transcription factors that play key roles in the control of growth and differentiation in reproductive tissues. We showed that the novel Dbl family proto-oncoprotein Brx enhances ligand-dependent activity of ERalpha via a Cdc42-dependent pathway. Brx also significantly enhances ligand-dependent activity of ERbeta . This enhancement is not affected by inhibition of p44/42 mitogen-activated protein kinase (MAPK) activation by PD98059. However, addition of the p38 MAPK inhibitor SB202190 abrogates the enhancement of ERbeta activity by Brx, showing that p38 MAPK activity is required for the enhancement of ERbeta function by Brx. In COS-7 cells, transfection of Brx leads to activation of endogenous p38 MAPK activity. Co-expression of the beta 2 isoform of human p38 MAPK and a constitutively active form of the p38 MAPK kinase MKK6 (MKK6-EE) synergistically augments ligand-dependent activity of ERbeta . Our findings suggest that p38 MAPKs may be important regulators of ERbeta activity.

* This work was supported by grants from the Uniformed Services University of the Health Sciences, the Elsa U. Pardee Foundation, and the Department of Defense Breast Cancer Research program.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ First and senior author. To whom correspondence should be addressed: Dept. of Obstetrics and Gynecology, Uniformed Services University of the Health Sciences, 4301 Jones Bridge Rd., Bethesda, MD 20814. Tel.: 301-295-3777; Fax: 301-295-6774; E-mail: pdriggers@rocketmail.com.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Mol. Endocrinol.Home page
N. Picard, C. Charbonneau, M. Sanchez, A. Licznar, M. Busson, G. Lazennec, and A. Tremblay
Phosphorylation of Activation Function-1 Regulates Proteasome-Dependent Nuclear Mobility and E6-Associated Protein Ubiquitin Ligase Recruitment to the Estrogen Receptor {beta}
Mol. Endocrinol., February 1, 2008; 22(2): 317 - 330.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
O. Shibolet, C. Giallourakis, I. Rosenberg, T. Mueller, R. J. Xavier, and D. K. Podolsky
AKAP13, a RhoA GTPase-specific Guanine Exchange Factor, Is a Novel Regulator of TLR2 Signaling
J. Biol. Chem., November 30, 2007; 282(48): 35308 - 35317.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Sanchez, K. Sauve, N. Picard, and A. Tremblay
The Hormonal Response of Estrogen Receptor beta Is Decreased by the Phosphatidylinositol 3-Kinase/Akt Pathway via a Phosphorylation-dependent Release of CREB-binding Protein
J. Biol. Chem., February 16, 2007; 282(7): 4830 - 4840.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Q. Lin, W. Yang, D. Baird, Q. Feng, and R. A. Cerione
Identification of a DOCK180-related Guanine Nucleotide Exchange Factor That Is Capable of Mediating a Positive Feedback Activation of Cdc42
J. Biol. Chem., November 17, 2006; 281(46): 35253 - 35262.
[Abstract] [Full Text] [PDF]

Home page
 Cancer Res.Home page
B. N. Duong, S. Elliott, D. E. Frigo, L. I. Melnik, L. Vanhoy, S. Tomchuck, H. P. Lebeau, O. David, B. S. Beckman, J. Alam, et al.
AKT Regulation of Estrogen Receptor {beta} Transcriptional Activity in Breast Cancer.
Cancer Res., September 1, 2006; 66(17): 8373 - 8381.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Endocrinol.Home page
D. E. Frigo, A. Basu, E. N. Nierth-Simpson, C. B. Weldon, C. M. Dugan, S. Elliott, B. M. Collins-Burow, V. A. Salvo, Y. Zhu, L. I. Melnik, et al.
p38 Mitogen-Activated Protein Kinase Stimulates Estrogen-Mediated Transcription and Proliferation through the Phosphorylation and Potentiation of the p160 Coactivator Glucocorticoid Receptor-Interacting Protein 1
Mol. Endocrinol., May 1, 2006; 20(5): 971 - 983.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Kino, E. Souvatzoglou, E. Charmandari, T. Ichijo, P. Driggers, C. Mayers, A. Alatsatianos, I. Manoli, H. Westphal, G. P. Chrousos, et al.
Rho Family Guanine Nucleotide Exchange Factor Brx Couples Extracellular Signals to the Glucocorticoid Signaling System
J. Biol. Chem., April 7, 2006; 281(14): 9118 - 9126.
[Abstract] [Full Text] [PDF]

Home page
 CarcinogenesisHome page
M. Wirtenberger, S. Tchatchou, K. Hemminki, R. Klaes, R. K. Schmutzler, J. L. Bermejo, B. Chen, B. Wappenschmidt, A. Meindl, C. R. Bartram, et al.
Association of genetic variants in the Rho guanine nucleotide exchange factor AKAP13 with familial breast cancer
Carcinogenesis, March 1, 2006; 27(3): 593 - 598.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. M. Coleman, M. Dutertre, A. El-Gharbawy, B. G. Rowan, N. L. Weigel, and C. L. Smith
Mechanistic Differences in the Activation of Estrogen Receptor-alpha (ERalpha )- and ERbeta -dependent Gene Expression by cAMP Signaling Pathway(s)
J. Biol. Chem., April 4, 2003; 278(15): 12834 - 12845.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.